LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 7 of total 7

Search options

  1. Article ; Online: Genetic Analysis Reveals a Requirement for the Hybrid Sensor Kinase RscS in

    Dial, Courtney N / Fung, Brittany L / Visick, Karen L

    Journal of bacteriology

    2023  Volume 205, Issue 7, Page(s) e0007523

    Abstract: The marine bacterium Vibrio fischeri initiates symbiotic colonization of its squid host, ...

    Abstract The marine bacterium Vibrio fischeri initiates symbiotic colonization of its squid host,
    MeSH term(s) Humans ; 4-Aminobenzoic Acid/metabolism ; Calcium/metabolism ; Aliivibrio fischeri/genetics ; Bacterial Proteins/genetics ; Biofilms ; Phosphotransferases/metabolism
    Chemical Substances 4-Aminobenzoic Acid (TL2TJE8QTX) ; Calcium (SY7Q814VUP) ; Bacterial Proteins ; Phosphotransferases (EC 2.7.-)
    Language English
    Publishing date 2023-06-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00075-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Coxsackievirus B3 Responds to Polyamine Depletion via Enhancement of 2A and 3C Protease Activity.

    Dial, Courtney N / Tate, Patrick M / Kicmal, Thomas M / Mounce, Bryan C

    Viruses

    2019  Volume 11, Issue 5

    Abstract: Polyamines are small positively-charged molecules abundant in eukaryotic cells that are crucial to RNA virus replication. In eukaryotic cells, polyamines facilitate processes such as transcription, translation, and DNA replication, and viruses similarly ... ...

    Abstract Polyamines are small positively-charged molecules abundant in eukaryotic cells that are crucial to RNA virus replication. In eukaryotic cells, polyamines facilitate processes such as transcription, translation, and DNA replication, and viruses similarly rely on polyamines to facilitate transcription and translation. Whether polyamines function at additional stages in viral replication remains poorly understood. Picornaviruses, including Coxsackievirus B3 (CVB3), are sensitive to polyamine depletion both in vitro and in vivo; however, precisely how polyamine function in picornavirus infection has not been described. Here, we describe CVB3 mutants that arise with passage in polyamine-depleted conditions. We observe mutations in the 2A and 3C proteases, and we find that these mutant proteases confer resistance to polyamine depletion. Using a split luciferase reporter system to measure protease activity, we determined that polyamines facilitate viral protease activity. We further observe that the 2A and 3C protease mutations enhance reporter protease activity in polyamine-depleted conditions. Finally, we find that these mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells. In sum, our results suggest that polyamines are crucial to protease function during picornavirus infection. Further, these data highlight viral proteases as potential antiviral targets and highlight how CVB3 may overcome polyamine-depleting antiviral therapies.
    MeSH term(s) 3C Viral Proteases ; Animals ; Cell Line ; Cells, Cultured ; Chlorocebus aethiops ; Coxsackievirus Infections/metabolism ; Coxsackievirus Infections/virology ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Enterovirus B, Human/physiology ; Enzyme Activation ; Enzyme Stability ; Host-Pathogen Interactions ; Humans ; Mutation ; Polyamines/metabolism ; Proteolysis ; Vero Cells ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Polyamines ; Viral Proteins ; Cysteine Endopeptidases (EC 3.4.22.-) ; 3C Viral Proteases (EC 3.4.22.28) ; picornain 2A, Picornavirus (EC 3.4.22.29)
    Keywords covid19
    Language English
    Publishing date 2019-04-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v11050403
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: Coxsackievirus B3 Responds to Polyamine Depletion via Enhancement of 2A and 3C Protease Activity

    Dial, Courtney N / Tate, Patrick M / Kicmal, Thomas M / Mounce, Bryan C

    Viruses. 2019 Apr. 30, v. 11, no. 5

    2019  

    Abstract: Polyamines are small positively-charged molecules abundant in eukaryotic cells that are crucial to RNA virus replication. In eukaryotic cells, polyamines facilitate processes such as transcription, translation, and DNA replication, and viruses similarly ... ...

    Abstract Polyamines are small positively-charged molecules abundant in eukaryotic cells that are crucial to RNA virus replication. In eukaryotic cells, polyamines facilitate processes such as transcription, translation, and DNA replication, and viruses similarly rely on polyamines to facilitate transcription and translation. Whether polyamines function at additional stages in viral replication remains poorly understood. Picornaviruses, including Coxsackievirus B3 (CVB3), are sensitive to polyamine depletion both in vitro and in vivo; however, precisely how polyamine function in picornavirus infection has not been described. Here, we describe CVB3 mutants that arise with passage in polyamine-depleted conditions. We observe mutations in the 2A and 3C proteases, and we find that these mutant proteases confer resistance to polyamine depletion. Using a split luciferase reporter system to measure protease activity, we determined that polyamines facilitate viral protease activity. We further observe that the 2A and 3C protease mutations enhance reporter protease activity in polyamine-depleted conditions. Finally, we find that these mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells. In sum, our results suggest that polyamines are crucial to protease function during picornavirus infection. Further, these data highlight viral proteases as potential antiviral targets and highlight how CVB3 may overcome polyamine-depleting antiviral therapies.
    Keywords DNA replication ; Picornaviridae ; enzyme activity ; eukaryotic cells ; luciferase ; mutants ; mutation ; polyamines ; proteinases ; transcription (genetics) ; translation (genetics) ; virus replication ; viruses ; covid19
    Language English
    Dates of publication 2019-0430
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v11050403
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Para-Aminobenzoic Acid, Calcium, and c-di-GMP Induce Formation of Cohesive, Syp-Polysaccharide-Dependent Biofilms in Vibrio fischeri.

    Dial, Courtney N / Speare, Lauren / Sharpe, Garrett C / Gifford, Scott M / Septer, Alecia N / Visick, Karen L

    mBio

    2021  Volume 12, Issue 5, Page(s) e0203421

    Abstract: The marine bacterium Vibrio fischeri efficiently colonizes its symbiotic squid host, Euprymna scolopes, by producing a transient biofilm dependent on the symbiosis polysaccharide (SYP). ...

    Abstract The marine bacterium Vibrio fischeri efficiently colonizes its symbiotic squid host, Euprymna scolopes, by producing a transient biofilm dependent on the symbiosis polysaccharide (SYP).
    MeSH term(s) 4-Aminobenzoic Acid/metabolism ; Aliivibrio fischeri/genetics ; Aliivibrio fischeri/growth & development ; Aliivibrio fischeri/metabolism ; Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms ; Calcium/metabolism ; Cyclic GMP/analogs & derivatives ; Cyclic GMP/metabolism ; Decapodiformes/microbiology ; Decapodiformes/physiology ; Gene Expression Regulation, Bacterial ; Polysaccharides, Bacterial/metabolism ; Symbiosis
    Chemical Substances Bacterial Proteins ; Polysaccharides, Bacterial ; bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Cyclic GMP (H2D2X058MU) ; Calcium (SY7Q814VUP) ; 4-Aminobenzoic Acid (TL2TJE8QTX)
    Language English
    Publishing date 2021-10-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.02034-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Quorum Sensing and Cyclic di-GMP Exert Control Over Motility of

    Dial, Courtney N / Eichinger, Steven J / Foxall, Randi / Corcoran, Christopher J / Tischler, Alice H / Bolz, Robert M / Whistler, Cheryl A / Visick, Karen L

    Frontiers in microbiology

    2021  Volume 12, Page(s) 690459

    Abstract: Bacterial motility is critical for symbiotic colonization ... ...

    Abstract Bacterial motility is critical for symbiotic colonization by
    Language English
    Publishing date 2021-06-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2021.690459
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Polyamine Depletion Abrogates Enterovirus Cellular Attachment.

    Kicmal, Thomas M / Tate, Patrick M / Dial, Courtney N / Esin, Jeremy J / Mounce, Bryan C

    Journal of virology

    2019  Volume 93, Issue 20

    Abstract: Polyamines are small polycationic molecules with flexible carbon chains that are found in all eukaryotic cells. Polyamines are involved in the regulation of many host processes and have been shown to be implicated in viral replication. Depletion of ... ...

    Abstract Polyamines are small polycationic molecules with flexible carbon chains that are found in all eukaryotic cells. Polyamines are involved in the regulation of many host processes and have been shown to be implicated in viral replication. Depletion of polyamine pools in cells treated with FDA-approved drugs restricts replication of diverse RNA viruses. Viruses can exploit host polyamines to facilitate nucleic acid packaging, transcription, and translation, but other mechanisms remain largely unknown. Picornaviruses, including Coxsackievirus B3 (CVB3), are sensitive to the depletion of polyamines and remain a significant public health threat. We employed CVB3 as a model system to investigate a potential proviral role for polyamines using a forward screen. Passaging CVB3 in polyamine-depleted cells generated a mutation in capsid protein VP3 at residue 234. We show that this mutation confers resistance to polyamine depletion. Through attachment assays, we demonstrate that polyamine depletion limits CVB3 attachment to susceptible cells, which is rescued by incubating virus with polyamines. Furthermore, the capsid mutant rescues this inhibition in polyamine-depleted cells. More divergent viruses also exhibited reduced attachment to polyamine-depleted cells, suggesting that polyamines may facilitate attachment of diverse RNA viruses. These studies inform additional mechanisms of action for polyamine-depleting pharmaceuticals, with implications for potential antiviral therapies.
    MeSH term(s) Animals ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Chlorocebus aethiops ; Enterovirus/physiology ; Enterovirus Infections/metabolism ; Enterovirus Infections/virology ; Humans ; Mutation ; Polyamines/metabolism ; Vero Cells ; Virus Attachment ; Virus Replication
    Chemical Substances Capsid Proteins ; Polyamines
    Language English
    Publishing date 2019-09-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01054-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Polyamine Depletion Inhibits Bunyavirus Infection via Generation of Noninfectious Interfering Virions.

    Mastrodomenico, Vincent / Esin, Jeremy J / Graham, Marion L / Tate, Patrick M / Hawkins, Grant M / Sandler, Zachary J / Rademacher, David J / Kicmal, Thomas M / Dial, Courtney N / Mounce, Bryan C

    Journal of virology

    2019  Volume 93, Issue 14

    Abstract: Several host and viral processes contribute to forming infectious virions. Polyamines are small host molecules that play diverse roles in viral replication. We previously demonstrated that polyamines are crucial for RNA viruses; however, the mechanisms ... ...

    Abstract Several host and viral processes contribute to forming infectious virions. Polyamines are small host molecules that play diverse roles in viral replication. We previously demonstrated that polyamines are crucial for RNA viruses; however, the mechanisms by which polyamines function remain unknown. Here, we investigated the role of polyamines in the replication of the bunyaviruses Rift Valley fever virus (vaccine strain MP-12) and La Crosse virus (LACV). We found that polyamine depletion did not impact viral RNA or protein accumulation, despite significant decreases in titer. Viral particles demonstrated no change in morphology, size, or density. Thus, polyamine depletion promotes the formation of noninfectious particles. These particles interfere with virus replication and stimulate innate immune responses. We extended this phenotype to Zika virus; however, coxsackievirus did not similarly produce noninfectious particles. In sum, polyamine depletion results in the accumulation of noninfectious particles that interfere with replication and stimulate immune signaling, with important implications for targeting polyamines therapeutically, as well as for vaccine strategies.
    MeSH term(s) Biogenic Polyamines/immunology ; Bunyaviridae Infections/genetics ; Bunyaviridae Infections/immunology ; Bunyaviridae Infections/pathology ; Cell Line, Tumor ; Defective Viruses/physiology ; Encephalitis Virus, California/physiology ; Humans ; Rift Valley fever virus/physiology ; Virion/physiology ; Virus Replication/immunology
    Chemical Substances Biogenic Polyamines
    Language English
    Publishing date 2019-06-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.00530-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top